The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.
You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.
We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.
We are interested in where in or outside the cell the gene product carries out its function.
We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.
Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.
Extensive recent literature confirms that the gene product identified as TLR15 (UniProt: A0A8V0Z0H8) is correctly annotated as a chicken (Gallus gallus) Toll-like receptor, member of the TLR family, with characteristic domains: extracellular leucine-rich repeats (LRR), a single transmembrane region, and an intracellular Toll/IL-1 receptor (TIR) domain. The protein product's structure and biological function correspond with database annotation and all recent research collected, and there is no conflict with other proteins sharing the same symbol (neerukonda2020avianpatternrecognition pages 9-11, neves2022uncoveringa500 pages 2-4).
TLR15 is an avian- and reptile-lineage-specific pattern recognition receptor (PRR) that is most robustly present in birds, including chicken, but absent from mammals. It is localized primarily at the cell surface/plasma membrane of immune (macrophages, dendritic cells) and non-immune (epithelial) cells, where it surveils for pathogen intrusion (neerukonda2020avianpatternrecognition pages 9-11). Unlike most TLRs that directly recognize defined molecular patterns, TLR15 is activated by proteolytic cleavage—most notably by proteases secreted by pathogenic bacteria, fungi, and some parasites. This mechanism is unique among TLRs studied in vertebrates and highlights a dedicated role for detection of extracellular protease activity as a danger signal (neerukonda2020avianpatternrecognition pages 3-6, neerukonda2020avianpatternrecognition pages 9-11).
Recently resolved high-resolution crystal structures (PDB: 7YLF, 7YLG) revealed the atomic details of TLR15’s intracellular TIR domain, including unique features (extended BB and DD loops, C2 helix) critical for signaling dimer formation. Structural studies confirm the pathway proceeds via MyD88-dependent activation (ko2023structuralanalysisof pages 3-4, ko2023structuralanalysisof pages 1-2).
In 2025, the aspartyl protease EteASP from the coccidial parasite Eimeria tenella was identified as a direct candidate TLR15 ligand. Recombinant EteASP was shown to activate chicken macrophages and dendritic cells, stimulating NF-κB and MAPK signaling cascades, the NLRP3 inflammasome, and driving production of cytokines (IL-1β, IL-6, TNF-α), nitric oxide, and reactive oxygen species (chen2025eimeriatenellaaspartyl pages 1-2, chen2025eimeriatenellaaspartyl pages 8-11). Induction of the same signaling axis has since been corroborated in sporozoite-challenged chicken fibroblasts and in vivo infection models (li2021activationofchtlr15chnfκbchnlrp3chil1β pages 1-2, li2021activationofchtlr15chnfκbchnlrp3chil1β pages 7-9).
Other recognized stimuli include microbial proteases from Salmonella, Enterococcus, Mycoplasma synoviae (diacylated lipopeptide), and possibly yeast-derived lipoproteins, though the latter are less directly established (mehrzad2024avianinnateand pages 6-8, neerukonda2020avianpatternrecognition pages 9-11, rehman2021thepotentialof pages 2-3).
Upon receptor activation at the plasma membrane, TLR15 initiates a cascade involving the MyD88 adaptor, leading to strong NF-κB and MAPK activation, subsequently stimulating the NLRP3 inflammasome/caspase-1 axis and release of IL-1β and IL-18. This results in enhanced macrophage/dendritic cell activation, phagocytosis, and pro-inflammatory mediator and nitric oxide production (neerukonda2020avianpatternrecognition pages 9-11, chen2025eimeriatenellaaspartyl pages 1-2, li2021activationofchtlr15chnfκbchnlrp3chil1β pages 1-2).
TLR15 is expressed in several immune tissues (spleen, bursa of Fabricius, bone marrow, cecum, ileum) and non-immune tissues, and its expression is inducible upon pathogen challenge and during development. Upregulation is observed in the cecum post-Eimeria and Salmonella infection, ileum and spleen during necrotic enteritis, and in response to Mycoplasma and various stresses (mehrzad2024avianinnateand pages 6-8, neerukonda2020avianpatternrecognition pages 9-11, cader2023activationoftolllike pages 41-46, rehman2021thepotentialof pages 5-6).
Given its protease-driven recognition mechanism, TLR15 is investigated as a model for adjuvants and feed additives that could augment or mimic protease stimulus, potentially improving disease resistance in commercial poultry (rehman2021thepotentialof pages 2-3).
Integrative summaries below capture the most authoritative and current data.
| Property | Current annotation and evidence | Evidence strength / caveat |
|---|---|---|
| Identity | TLR15 (Toll-like receptor 15) from Gallus gallus; UniProt accession A0A8V0Z0H8. The literature describes the same chicken TLR15 protein family and domain architecture specified by UniProt. | Identity is well supported; no conflicting same-symbol protein was identified. |
| Protein class and primary function | Single-pass Toll-like pattern-recognition receptor specialized for detecting extracellular microbial proteolytic activity and initiating innate inflammatory signaling. It is a signaling receptor, not an enzyme or transporter. (neerukonda2020avianpatternrecognition pages 3-6, neerukonda2020avianpatternrecognition pages 9-11) | High confidence for protease sensing; broader claims of direct recognition of lipoproteins or yeast products are less mechanistically established. |
| Domain architecture | Canonical type-I TLR organization: N-terminal signal peptide, extracellular leucine-rich-repeat (LRR) ectodomain, one transmembrane helix, and a cytoplasmic Toll/IL-1 receptor (TIR) domain. This agrees with the supplied InterPro assignments: IPR001611, IPR003591, IPR032675, IPR000157 and IPR035897. (neerukonda2020avianpatternrecognition pages 9-11, neves2022uncoveringa500 pages 2-4) | Strong family-level and sequence-domain support; the complete full-length ectodomain has not been structurally resolved. |
| TIR-domain structure | The crystallized chicken TIR construct encompassed residues 699–868; resolved structures contained residues 704–788 and 793–850. The domain has a central five-stranded β-sheet surrounded by α-helices and an unusual BB loop, DD loop and C2 helix. Structures were solved at 1.90 Å and 1.80 Å resolution (PDB 7YLF and 7YLG). (ko2023structuralanalysisof pages 3-4, ko2023structuralanalysisof pages 1-2) | High-confidence atomic structural evidence for the intracellular domain. |
| Receptor oligomerization | TLR15 can form homodimers. The crystallographic TIR dimer buries about 1,110 Ų per monomer; the C2 region contributes about 59% and the BB region about 30% of the interface. Ile753, Tyr779 and Phe813 contribute to dimerization; Y779D eliminated the detectable dimer peak. (ko2023structuralanalysisof pages 7-9, ko2023structuralanalysisof pages 4-7) | Strong structural and mutational support for a plausible signaling dimer, although the isolated TIR domain is predominantly monomeric in solution. |
| Cellular localization | Chicken TLR15 is principally a cell-surface/plasma-membrane receptor, positioning its LRR ectodomain to encounter extracellular pathogen proteases. This contrasts with endosomal avian TLR3, TLR7 and TLR21 and with reported intracellular localization of some reptilian TLR15 orthologs. (neerukonda2020avianpatternrecognition pages 9-11, magor2022evolutionofrna pages 4-5) | Good experimental and review support; trafficking dynamics after cleavage remain incompletely defined. |
| Best-established activating signal | Proteases from bacteria and fungi cleave the extracellular LRR region, generating an approximately 70-kDa C-terminal fragment. Cleavage is inhibited by PMSF, consistent with serine-protease involvement. Removal of inhibitory ectodomain elements is proposed to permit receptor self-activation. (neerukonda2020avianpatternrecognition pages 9-11) | High confidence that proteolysis activates the receptor; the precise cleavage site and complete conformational sequence remain unresolved. |
| Candidate non-protease stimuli | Yeast-associated lipoprotein or lysate and a Mycoplasma synoviae diacylated lipopeptide have been associated with TLR15 responses. M. synoviae stimulation induced TLR15, iNOS and nitric oxide, and these responses declined after TLR15-targeted siRNA. (mehrzad2024avianinnateand pages 6-8, neerukonda2020avianpatternrecognition pages 9-11) | Functional association is supported, but direct physical binding and receptor exclusivity are not established; these stimuli may involve receptor cooperation or indirect induction. |
| Parasite-derived candidate ligand | A 2025 study identified Eimeria tenella aspartyl protease (EteASP) as a candidate TLR15-interacting ligand by co-immunoprecipitation. Recombinant EteASP activated chicken macrophages and bone-marrow-derived dendritic cells. (chen2025eimeriatenellaaspartyl pages 1-2, chen2025eimeriatenellaaspartyl pages 8-11) | Important recent finding, but the authors describe TLR15 as a potential receptor; contributions from other PRRs remain possible. |
| Proximal signaling | Proteolytic activation and TIR-domain dimerization support recruitment of the adaptor MyD88, followed by activation of NF-κB. The conserved, solvent-exposed BB-loop proline is structurally compatible with MyD88-dependent signaling. (neerukonda2020avianpatternrecognition pages 9-11, ko2023structuralanalysisof pages 9-10) | MyD88 dependence is well supported; a direct atomic structure of the TLR15–MyD88 complex is unavailable. |
| Extended signaling pathways | In E. tenella models, TLR15 activation is coupled to NF-κB → NLRP3 → caspase-1 → IL-1β/IL-18 signaling. EteASP also activates MAPK signaling. Overexpression of TLR15 enhanced, and knockdown reduced, pathway activation in DF-1 cells exposed to sporozoites. (chen2025eimeriatenellaaspartyl pages 1-2, li2021activationofchtlr15chnfκbchnlrp3chil1β pages 1-2, li2021activationofchtlr15chnfκbchnlrp3chil1β pages 7-9) | Strong pathway-level evidence in infection and cell models; not every downstream branch has been proven to arise from direct TLR15 activation in all cell types. |
| Downstream effectors | Documented or closely associated outputs include NF-κB activation, NLRP3 and caspase-1 activity, IL-1β, IL-6, IL-18 and TNF-α production, iNOS induction, nitric oxide and reactive oxygen species. EteASP additionally increased macrophage phagocytosis and dendritic-cell CD11c and MHC-II expression. (neerukonda2020avianpatternrecognition pages 9-11, chen2025eimeriatenellaaspartyl pages 1-2) | Cytokine specificity varies by stimulus and model; IL-6, TNF-α, ROS and antigen-presentation effects derive particularly from the candidate EteASP study. |
| Baseline and inducible tissue distribution | Expression has been reported in spleen, bursa of Fabricius, bone marrow and intestine. Infection-associated expression occurs in cecum, ileum and spleen; demonstrated responding cells include chicken embryo fibroblasts, HD11 macrophages, primary chondrocytes, macrophages and bone-marrow-derived dendritic cells. (mehrzad2024avianinnateand pages 6-8, neerukonda2020avianpatternrecognition pages 9-11, cader2023activationoftolllike pages 41-46) | Broad tissue expression is supported, but quantitative baseline protein-level maps and single-cell localization remain limited. |
| Eimeria tenella response | Cecal TLR15, MyD88, NF-κB, NLRP3, caspase-1, IL-1β and IL-18 increased significantly at 4, 12 and 24 hours after infection; sporozoite-stimulated DF-1 cells reproduced the pathway response. A later study found cecal TLR15 negatively correlated with oocyst output, whereas splenic expression correlated positively. (zhu2026tolllikereceptormediatedinnate pages 1-2, li2021activationofchtlr15chnfκbchnlrp3chil1β pages 1-2) | Mechanistic evidence supports inflammatory involvement; expression correlations do not by themselves establish protection or causation. |
| Bacterial-pathogen responses | TLR15 is induced in the cecum during Salmonella enterica serovar Typhimurium infection and in fibroblasts exposed to heat-killed bacteria. It is also induced by M. synoviae or its diacylated lipopeptide and is upregulated in ileum and spleen during Clostridium perfringens-associated necrotic enteritis. (neerukonda2020avianpatternrecognition pages 9-11, rehman2021thepotentialof pages 5-6) | These findings establish responsiveness, not necessarily direct recognition of a pathogen-specific molecule in every case. Salmonella and C. perfringens should not automatically be treated as proven direct TLR15 ligands. |
| Viral associations | TLR15 expression changes have been reported during some avian viral infections, including splenic upregulation with fowl adenovirus 8b; however, TLR15 is not established as a direct viral nucleic-acid sensor. (zhu2026tolllikereceptormediatedinnate pages 1-2) | Primarily expression-level association; direct viral ligand recognition and antiviral mechanism remain uncertain. |
| Evolutionary distribution | TLR15 is absent from mammals but retained broadly in birds and some reptiles. Comparative genomic work extends its origin to the common ancestor of jawed vertebrates more than 450 million years ago, with orthologs in lungfish and holocephalan cartilaginous fishes and extensive lineage-specific loss or pseudogenization elsewhere. (neves2022uncoveringa500 pages 1-2, neves2022uncoveringa500 pages 4-6, neves2022uncoveringa500 pages 2-4) | The older description “avian-specific” is operationally useful in poultry immunology but phylogenetically incomplete; current evidence supports an ancient, patchily retained vertebrate lineage. |
| Functional interpretation | The most defensible annotation is: cell-surface innate immune receptor activated by pathogen-associated extracellular proteolysis, signaling mainly through TIR–MyD88–NF-κB and, in relevant infection contexts, MAPK and NLRP3-inflammasome pathways. (neerukonda2020avianpatternrecognition pages 9-11, li2021activationofchtlr15chnfκbchnlrp3chil1β pages 1-2) | High-confidence core annotation; exact protease specificity, cleavage site, co-receptors and stimulus-dependent pathway branching remain research gaps. |
Table: This table integrates structural, localization, ligand, signaling, expression, pathogen-response and evolutionary evidence for chicken TLR15. It distinguishes experimentally established functions from candidate ligands and expression-only associations.
| Pathogen | Disease / challenge | Tissue or cell model | TLR15 change or activation | Associated immune response | Functional / clinical significance |
|---|---|---|---|---|---|
| Eimeria tenella | Cecal coccidiosis | Cecum; DF-1 chicken fibroblasts exposed to sporozoites | TLR15 mRNA and protein increased significantly at 4, 12, and 24 h after infection; overexpression enhanced, whereas knockdown suppressed, downstream signaling | MyD88–NF-κB activation followed by NLRP3–caspase-1 signaling and increased IL-1β and IL-18; establishes a causal contribution to the early inflammatory response (li2021activationofchtlr15chnfκbchnlrp3chil1β pages 1-2, li2021activationofchtlr15chnfκbchnlrp3chil1β pages 7-9) | Strongest pathogen-specific mechanistic evidence for TLR15. Cecal TLR15 expression was also negatively correlated with oocyst output, consistent with—but not proving—a locally protective role (zhu2026tolllikereceptormediatedinnate pages 1-2) |
| E. tenella aspartyl protease (EteASP) | Parasite-derived molecular challenge relevant to coccidiosis | Chicken macrophages and bone-marrow-derived dendritic cells | EteASP was recovered as a candidate TLR15-interacting ligand by co-immunoprecipitation; recombinant EteASP also increased TLR15 transcription in dendritic cells | Activated NF-κB and MAPK; increased IL-1β, IL-6, TNF-α, nitric oxide, reactive oxygen species, macrophage phagocytosis, CD11c and MHC-II expression, and naïve-T-cell activation (chen2025eimeriatenellaaspartyl pages 1-2, chen2025eimeriatenellaaspartyl pages 8-11) | Identifies a possible parasite-derived TLR15 agonist and prospective immunostimulant, but direct and exclusive receptor dependence remains unproven because other pattern-recognition receptors may contribute |
| Salmonella enterica serovar Typhimurium | Salmonellosis / intestinal bacterial challenge | Cecum in infected chickens; chicken embryo fibroblasts exposed to heat-killed bacteria | TLR15 transcription was significantly upregulated in infected cecum and induced by heat-killed bacteria; these data show responsiveness but do not establish Salmonella as a direct TLR15 ligand | Consistent with cell-surface protease sensing and MyD88-dependent NF-κB inflammatory signaling; the precise TLR15-specific cytokine profile was not resolved (neerukonda2020avianpatternrecognition pages 9-11) | Supports TLR15 as an inducible component of intestinal antibacterial defense; functional effects on bacterial clearance or disease severity remain to be demonstrated |
| Clostridium perfringens | Necrotic enteritis | Ileum and spleen | Infection increased TLR15 expression together with TLR2-family genes and TLR21 | Associated with TLR/NF-κB inflammatory signaling and TNF-α production, although these outputs were not isolated experimentally as TLR15-specific (rehman2021thepotentialof pages 5-6) | Implicates TLR15 in local intestinal and systemic responses to necrotic enteritis; whether activation is protective or contributes to damaging inflammation is unresolved |
| Mycoplasma synoviae and its diacylated lipopeptide | Infectious synovitis / mycoplasmosis | HD11 chicken macrophages and primary chondrocytes | Infection or diacylated-lipopeptide exposure induced TLR15; TLR15-targeting siRNA reduced associated responses | Increased inducible nitric-oxide synthase and nitric-oxide production; knockdown evidence supports a functional TLR15 contribution (neerukonda2020avianpatternrecognition pages 9-11) | Provides receptor-dependence evidence for antimicrobial inflammatory signaling in immune cells and joint-associated chondrocytes |
| Fowl adenovirus serotype 8b | Inclusion body hepatitis–associated viral infection | Spleen | Splenic TLR15 was reported to be significantly upregulated alongside TLR2 | Indicates participation in the innate response, but no direct viral ligand, TLR15-specific signaling mechanism, or causal antiviral effect was established (zhu2026tolllikereceptormediatedinnate pages 1-2) | TLR15 may serve as an infection-responsive marker; current evidence is transcriptional and does not establish it as a direct viral sensor |
| Viral infections more broadly | Newcastle disease and other avian viral challenges | Multiple tissues, depending on model | Some studies report altered TLR15 expression, but available evidence does not establish direct recognition of viral nucleic acids or proteins | Antiviral associations are likely indirect or context-dependent; canonical viral sensing in chickens is more firmly assigned to receptors such as TLR3 and TLR7 | TLR15 should not presently be annotated as a primary antiviral receptor; pathogen-associated protease sensing remains its best-supported molecular function (neerukonda2020avianpatternrecognition pages 3-6, neerukonda2020avianpatternrecognition pages 9-11) |
Table: This table distinguishes mechanistic evidence from expression-only associations across major chicken pathogens. It highlights especially strong causal support in Eimeria and Mycoplasma models while identifying unresolved roles in bacterial and viral disease.
See embedded tables for additional URLs and evidence details.
Chicken TLR15 is a uniquely positioned, cell-surface pattern-recognition receptor specializing in the detection of extracellular microbial proteolytic activity—bridging innate sensing to inflammation through MyD88–NF-κB–MAPK–NLRP3 axes. It provides a critical defense against protozoan, bacterial, and some viral poultry pathogens, with functional relevance that has been greatly clarified in the last 3–5 years. TLR15 serves not only as a biomarker for poultry health research, but as a model for understanding ancient and non-mammalian immune strategies, and as a potential target for immunomodulation in agriculture.
References
(neerukonda2020avianpatternrecognition pages 9-11): Sabari Nath Neerukonda and Upendra Katneni. Avian pattern recognition receptor sensing and signaling. Veterinary Sciences, 7:14, Jan 2020. URL: https://doi.org/10.3390/vetsci7010014, doi:10.3390/vetsci7010014. This article has 59 citations.
(neves2022uncoveringa500 pages 2-4): Fabiana Neves, Antonio Muñoz-Mérida, André M. Machado, Tereza Almeida, Arnaud Gaigher, Pedro J. Esteves, L. Filipe C. Castro, and Ana Veríssimo. Uncovering a 500 million year old history and evidence of pseudogenization for tlr15. Frontiers in Immunology, Dec 2022. URL: https://doi.org/10.3389/fimmu.2022.1020601, doi:10.3389/fimmu.2022.1020601. This article has 3 citations and is from a peer-reviewed journal.
(neerukonda2020avianpatternrecognition pages 3-6): Sabari Nath Neerukonda and Upendra Katneni. Avian pattern recognition receptor sensing and signaling. Veterinary Sciences, 7:14, Jan 2020. URL: https://doi.org/10.3390/vetsci7010014, doi:10.3390/vetsci7010014. This article has 59 citations.
(ko2023structuralanalysisof pages 3-4): Kyung Yeol Ko, Wan Seok Song, Jeongho Park, Geun-Shik Lee, and Sung-il Yoon. Structural analysis of the toll-like receptor 15 tir domain. IUCrJ, 10:352-362, Apr 2023. URL: https://doi.org/10.1107/s2052252523002956, doi:10.1107/s2052252523002956. This article has 5 citations and is from a peer-reviewed journal.
(ko2023structuralanalysisof pages 1-2): Kyung Yeol Ko, Wan Seok Song, Jeongho Park, Geun-Shik Lee, and Sung-il Yoon. Structural analysis of the toll-like receptor 15 tir domain. IUCrJ, 10:352-362, Apr 2023. URL: https://doi.org/10.1107/s2052252523002956, doi:10.1107/s2052252523002956. This article has 5 citations and is from a peer-reviewed journal.
(chen2025eimeriatenellaaspartyl pages 1-2): Chen Chen, Zhichao Men, Xianglin Pu, Mingmin Lu, Lixin Xu, Ruofeng Yan, Xiangrui Li, and Xiaokai Song. Eimeria tenella aspartyl protease is identified as a potential tlr15 ligand and activates macrophages and dendritic cells in chickens. Oct 2025. URL: https://doi.org/10.1016/j.psj.2025.105525, doi:10.1016/j.psj.2025.105525. This article has 3 citations and is from a peer-reviewed journal.
(chen2025eimeriatenellaaspartyl pages 8-11): Chen Chen, Zhichao Men, Xianglin Pu, Mingmin Lu, Lixin Xu, Ruofeng Yan, Xiangrui Li, and Xiaokai Song. Eimeria tenella aspartyl protease is identified as a potential tlr15 ligand and activates macrophages and dendritic cells in chickens. Oct 2025. URL: https://doi.org/10.1016/j.psj.2025.105525, doi:10.1016/j.psj.2025.105525. This article has 3 citations and is from a peer-reviewed journal.
(li2021activationofchtlr15chnfκbchnlrp3chil1β pages 1-2): Jian Li, Xuelian Yang, Zhipeng Jia, Chunli Ma, Xinghui Pan, and Dexing Ma. Activation of chtlr15/chnf-κb-chnlrp3/chil-1β signaling transduction pathway mediated inflammatory responses to e. tenella infection. Veterinary Research, Jan 2021. URL: https://doi.org/10.1186/s13567-020-00885-8, doi:10.1186/s13567-020-00885-8. This article has 18 citations and is from a highest quality peer-reviewed journal.
(li2021activationofchtlr15chnfκbchnlrp3chil1β pages 7-9): Jian Li, Xuelian Yang, Zhipeng Jia, Chunli Ma, Xinghui Pan, and Dexing Ma. Activation of chtlr15/chnf-κb-chnlrp3/chil-1β signaling transduction pathway mediated inflammatory responses to e. tenella infection. Veterinary Research, Jan 2021. URL: https://doi.org/10.1186/s13567-020-00885-8, doi:10.1186/s13567-020-00885-8. This article has 18 citations and is from a highest quality peer-reviewed journal.
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(rehman2021thepotentialof pages 2-3): Muhammad Saif-ur Rehman, Saif ur Rehman, Wasim Yousaf, Faiz-ul Hassan, Waqas Ahmad, Qingyou Liu, and Hongping Pan. The potential of toll-like receptors to modulate avian immune system: exploring the effects of genetic variants and phytonutrients. Frontiers in Genetics, Aug 2021. URL: https://doi.org/10.3389/fgene.2021.671235, doi:10.3389/fgene.2021.671235. This article has 64 citations and is from a peer-reviewed journal.
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(rehman2021thepotentialof pages 5-6): Muhammad Saif-ur Rehman, Saif ur Rehman, Wasim Yousaf, Faiz-ul Hassan, Waqas Ahmad, Qingyou Liu, and Hongping Pan. The potential of toll-like receptors to modulate avian immune system: exploring the effects of genetic variants and phytonutrients. Frontiers in Genetics, Aug 2021. URL: https://doi.org/10.3389/fgene.2021.671235, doi:10.3389/fgene.2021.671235. This article has 64 citations and is from a peer-reviewed journal.
(zhu2026tolllikereceptormediatedinnate pages 1-2): Huili Zhu, Guijie Zheng, Danni Wang, Qian Zhang, Yanhui Han, Song Wang, Qiangqiang Wang, Hongxuan He, Longxian Zhang, and Jianhe Hu. Toll-like receptor-mediated innate immune response correlate with the pathogenicity of eimeria tenella infection in spf chickens. Parasites & Vectors, May 2026. URL: https://doi.org/10.1186/s13071-026-07466-2, doi:10.1186/s13071-026-07466-2. This article has 0 citations and is from a peer-reviewed journal.
(neves2022uncoveringa500 pages 1-2): Fabiana Neves, Antonio Muñoz-Mérida, André M. Machado, Tereza Almeida, Arnaud Gaigher, Pedro J. Esteves, L. Filipe C. Castro, and Ana Veríssimo. Uncovering a 500 million year old history and evidence of pseudogenization for tlr15. Frontiers in Immunology, Dec 2022. URL: https://doi.org/10.3389/fimmu.2022.1020601, doi:10.3389/fimmu.2022.1020601. This article has 3 citations and is from a peer-reviewed journal.
(neves2022uncoveringa500 pages 4-6): Fabiana Neves, Antonio Muñoz-Mérida, André M. Machado, Tereza Almeida, Arnaud Gaigher, Pedro J. Esteves, L. Filipe C. Castro, and Ana Veríssimo. Uncovering a 500 million year old history and evidence of pseudogenization for tlr15. Frontiers in Immunology, Dec 2022. URL: https://doi.org/10.3389/fimmu.2022.1020601, doi:10.3389/fimmu.2022.1020601. This article has 3 citations and is from a peer-reviewed journal.
(ko2023structuralanalysisof pages 7-9): Kyung Yeol Ko, Wan Seok Song, Jeongho Park, Geun-Shik Lee, and Sung-il Yoon. Structural analysis of the toll-like receptor 15 tir domain. IUCrJ, 10:352-362, Apr 2023. URL: https://doi.org/10.1107/s2052252523002956, doi:10.1107/s2052252523002956. This article has 5 citations and is from a peer-reviewed journal.
(ko2023structuralanalysisof pages 4-7): Kyung Yeol Ko, Wan Seok Song, Jeongho Park, Geun-Shik Lee, and Sung-il Yoon. Structural analysis of the toll-like receptor 15 tir domain. IUCrJ, 10:352-362, Apr 2023. URL: https://doi.org/10.1107/s2052252523002956, doi:10.1107/s2052252523002956. This article has 5 citations and is from a peer-reviewed journal.
(ko2023structuralanalysisof pages 9-10): Kyung Yeol Ko, Wan Seok Song, Jeongho Park, Geun-Shik Lee, and Sung-il Yoon. Structural analysis of the toll-like receptor 15 tir domain. IUCrJ, 10:352-362, Apr 2023. URL: https://doi.org/10.1107/s2052252523002956, doi:10.1107/s2052252523002956. This article has 5 citations and is from a peer-reviewed journal.
(magor2022evolutionofrna pages 4-5): Katharine E. Magor. Evolution of rna sensing receptors in birds. Immunogenetics, 74:149-165, Jan 2022. URL: https://doi.org/10.1007/s00251-021-01238-1, doi:10.1007/s00251-021-01238-1. This article has 21 citations and is from a peer-reviewed journal.